Abstract:
:The analysis of the spectrum of circular dichroism (CD) of methionine-oxidized bovine parathyroid hormone peptide, bPTH(1-34) revealed that approximately 43% of the orderly conformation (alpha-helix and beta-sheet) was converted into random coil structure. This peptide failed to elicit any hypotensive response in rats at any of the tested doses from 0.01 to 0.05 mg/ml. The blue shift of tryptophan fluorescence and the increase in the fluorescence intensity of the fluorescence probe 2-p-toluidinylnaphthalene-6-sulfonate (TNS) bound to the oxidized peptide indicated that the more hydrophobic environment was generated in the tryptophan domain as well as the molecule as a whole when the methionines in the peptide were oxidized. Modification of arginine with 1,2-cyclohexanedione (CHD) reduced 30% to 50% of the hypotensive action of the peptide hormone. Similar results in the increase of hydrophobicity of the arginine-modified peptide were also observed. These studies suggest that the conformational changes due to the methionine oxidation or arginine modification may be related to the inactivation of the vascular activity of bPTH(1-34).
journal_name
Peptidesjournal_title
Peptidesauthors
Hong BS,Yang MC,Liang JN,Pang PKdoi
10.1016/0196-9781(86)90143-9subject
Has Abstractpub_date
1986-11-01 00:00:00pages
1131-5issue
6eissn
0196-9781issn
1873-5169pii
0196-9781(86)90143-9journal_volume
7pub_type
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